Molecular Microbiology最新文献

{"title":"Distinct Spatial Organisation of Rho and RNA Polymerase in Salmonella Cells.","authors":"Lionello Bossi,Romain Le Bars,Johnathan C Black,Julia Buggiani,Caroline Clerté,Thuy Duong Do,Emmanuel Margeat,Marc Boudvillain,Nara Figueroa-Bossi","doi":"10.1111/mmi.70093","DOIUrl":"https://doi.org/10.1111/mmi.70093","url":null,"abstract":"Rho is a conserved, ATP-dependent RNA translocase that terminates transcription at hundreds of sites across bacterial genomes. Although the molecular mechanism of Rho-dependent termination is well characterized, its spatial interplay with RNA polymerase (RNAP) within bacterial cells remains elusive. To address this question, we constructed intragenic, in-frame fusions inserting mCherry or sfGFP 48 amino acid residues downstream of the N-terminus of Rho in Salmonella. Strikingly, mCherry-but not sfGFP-renders the first 48 residues of Rho dispensable. RhoΔ48::mCherry is viable in single copy and exhibits wild-type termination activity in vitro, whereas the full-length Rho::sfGFP fusion, although viable, slows growth and shows strongly reduced activity. Structured illumination microscopy (SIM) revealed that, despite these functional differences, both constructs exhibit similar localisation patterns relative to fluorescently tagged RNAP in single cells. During exponential growth, both Rho and RNAP form discrete clusters, but with markedly distinct spatial organisations: RNAP clusters associate with the nucleoid, whereas Rho is distributed throughout the cell body. This spatial partitioning persists in stationary phase, where RNAP becomes diffusely associated with a compacted nucleoid while Rho accumulates at the cell periphery. The widespread distribution of Rho at cytoplasmic locations is unexpected and suggests participation in cellular functions beyond its canonical role in transcription termination.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"62 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-06-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148342315","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Single‐Nucleotide Substitution Generates a de Novo Promoter That Activates a Latent Metabolic Bypass in Escherichia coli","authors":"Qiaoqiao Guo, Qi Zou, Jilong Qin, Makrina Totsika, Yaoqin Hong, John E. Cronan","doi":"10.1111/mmi.70092","DOIUrl":"https://doi.org/10.1111/mmi.70092","url":null,"abstract":"The <jats:styled-content style=\"fixed-case\"> <jats:italic>Escherichia coli</jats:italic> </jats:styled-content> <jats:italic>fabH</jats:italic> gene encodes the 3‐ketoacyl‐ACP synthase III that initiates fatty acid synthesis. Deletion of the <jats:italic>fabH</jats:italic> gene results in severely limited fatty acid synthesis and tiny cells that are unusually sensitive to antibiotics. Genetic investigations identified the <jats:italic>yiiD</jats:italic> gene, now called <jats:italic>madA</jats:italic> , that encodes a malonyl‐ACP decarboxylase that suppresses the <jats:italic>∆fabH</jats:italic> phenotype, but only when <jats:italic>madA</jats:italic> is multicopy. We selected vancomycin‐resistant suppressor derivatives of a <jats:italic>∆fabH</jats:italic> strain. Although such chromosomal mutations were generally rare and weak, suppressor strain s1 (a single C‐T transition) restored both wild‐type growth, high‐level vancomycin resistance, and wild‐type fatty acid synthesis by creation of a new promoter within the coding sequence of a gene upstream of <jats:italic>madA</jats:italic> . This provides a caveat to the extensive effort to develop FabH inhibitors as antibacterial drugs.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"6 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148321805","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Phosphorylation-Dependent Partner-Switching-Like Module Regulates a Glycosyltransferase Required for Heterocyst Polysaccharide Layer Formation in Anabaena sp. Strain PCC 7120.","authors":"Mai Harada,Satoshi Matsuoka,Shigeki Ehira","doi":"10.1111/mmi.70091","DOIUrl":"https://doi.org/10.1111/mmi.70091","url":null,"abstract":"Heterocyst-specific polysaccharide (Hep) is an essential component of the heterocyst envelope in the filamentous cyanobacterium Anabaena sp. PCC 7120; however, the regulatory mechanisms that control Hep layer formation remain poorly understood. Herein, we reveal that Hep layer formation is regulated by a phosphorylation-dependent partner-switching-like system involving the phosphatase HenR and the STAS domain-containing glycosyltransferase All4160. A nonphosphorylatable All4160 variant restores Hep formation in a henR disruptant, indicating that phosphorylation negatively regulates All4160 function. Using a bacterial two-hybrid assay, we identified two candidate kinases that interact with All4160, that is, Alr3423 and All2284, which phosphorylate All4160 in vitro. Genetic analysis revealed that deletion of alr3423, not all2284, suppresses the defect of the henR disruptant, indicating that Alr3423 plays a key role in regulating All4160 in vivo. This study identifies a phosphorylation switch that controls Hep layer formation and reveals a regulatory mechanism acting directly on a polysaccharide biosynthetic enzyme.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"157 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148299198","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Strict Aerobic Lifestyle and Anaerobic Survival of Bacteria: Inseparable Twins?","authors":"Meina Neumann-Schaal, José Manuel Borrero-de Acuña, Dieter Jahn","doi":"10.1111/mmi.70071","DOIUrl":"10.1111/mmi.70071","url":null,"abstract":"<p><p>For many decades the existence of strict aerobic bacteria was part of every textbook. However, considering habitats like soils or surfaces, many of these microorganisms are exposed to drastic changes in oxygen tension. A simple rain shower can change oxygen diffusion rates by a factor of 10.000. Thus, for many of the so-called strict aerobic bacteria, anaerobic growth and survival strategies were discovered, mainly relying on the use of alternative electron acceptors to oxygen, redox-active metabolites, or fermentation processes generating ATP at the substrate level. Survival without growth was recognized as an important lifestyle of bacteria. With the increasing availability of genome data, many highly diverse growth and survival strategies have become apparent in bacteria. But the overall picture is far from complete. Only recently, a novel puzzle piece of the anaerobic survival strategy of the opportunistic pathogen and model bacterium Pseudomonas aeruginosa in the absence of alternative electron acceptors was elucidated. It relies on the re-wiring of carbon flux away from the Entner-Doudoroff pathway towards the pentose-phosphate pathway and use of a phosphoketolase to allow for metabolic flux while preventing nonproductive NADH formation under these fermentation conditions and for ATP generation via acetate kinase.</p>","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":" ","pages":"546-551"},"PeriodicalIF":3.1,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147869027","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pseudomonas aeruginosa Relies on a Phosphoketolase to Support Anaerobic Survival Under Reductive Stress.","authors":"Richard D Horak, Nanqing Zhou, Korbinian O Thalhammer, Nathan F Dalleska, Ludmilla Aristilde, Dianne K Newman","doi":"10.1111/mmi.70059","DOIUrl":"10.1111/mmi.70059","url":null,"abstract":"<p><p>Across diverse contexts, bacteria experience loss of electron acceptors due to fluctuating environmental conditions, leading to growth-arrest and reductive stress. Yet, microbial metabolism has been primarily studied with cells growing under nutrient-replete conditions. To study how cells preserve metabolic flux under reductively stressed growth-arrest, we explored how the opportunistic pathogen Pseudomonas aeruginosa remodels its metabolism under such conditions. During anaerobic survival on glucose, P. aeruginosa utilizes the upper Embden-Meyerhoff-Parnas pathway and pentose-phosphate pathway to generate metabolite precursors for a previously undescribed phosphoketolase (herein termed xfp) used to produce acetyl-P and indirectly ATP via subsequent acetate formation. This re-routing bypasses P. aeruginosa's canonical glucose-catabolizing Entner-Doudoroff pathway (EDP), allowing for metabolic flux without exacerbating reductive stress. Moreover, anaerobic survival on diverse carbon sources triggers purine degradation and metabolite accumulation, requiring xfp to maintain metabolic balance and viability. Thus, our data suggest that phosphoketolases may play an additional role in ribonucleotide balance. This study expands our understanding of P. aeruginosa's anaerobic survival strategies and serves as a reminder that large gaps remain in our understanding of growth arrest physiology even in well-studied model organisms, highlighting the potential for basic discovery in the realm of non-growth metabolism.</p>","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":" ","pages":"361-374"},"PeriodicalIF":3.1,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13033310/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147307896","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"PLP Homeostasis Protein Is Required for Efficient Maturation of Aromatic Amino Acid Aminotransferase in Salmonella enterica","authors":"Brandi A. Buckner, Diana M. Downs","doi":"10.1111/mmi.70072","DOIUrl":"https://doi.org/10.1111/mmi.70072","url":null,"abstract":"Pyridoxal 5′‐phosphate (PLP) is an essential cofactor required for metabolic functions including amino acid biosynthesis. While the pathways of PLP synthesis are well characterized, it is unclear how newly synthesized PLP is delivered to apo PLP‐dependent enzymes (PLP‐DEs) in the cell. The highly conserved PLP Homeostasis Protein (PLPHP) is hypothesized to act as a PLP carrier that traffics the cofactor to PLP‐DEs. Prior studies have shown transfer of PLP between PLPHP homologs and PLP‐DEs in vitro. Data herein support a role for this transfer in vivo. This study utilizes a <jats:styled-content style=\"fixed-case\"> <jats:italic>Salmonella enterica</jats:italic> </jats:styled-content> mutant strain with a synthetic requirement for PLPHP homolog, YggS. Genetic and biochemical analyses suggest that the synthetic phenotype of a <jats:italic>yggS aspC</jats:italic> mutant results from inefficient maturation of the aromatic amino acid aminotransferase, TyrB. This requirement for YggS can be bypassed with accumulation of B <jats:sub>6</jats:sub> vitamer PMP, or upregulation of pyridoxal kinase (PdxK). Using TyrB as a target, we provide the first demonstration that YggS of <jats:styled-content style=\"fixed-case\"> <jats:italic>S. enterica</jats:italic> </jats:styled-content> can mediate transfer of PLP to a PLP‐DE in vitro. In total, this study defines multiple in vivo maturation pathways for TyrB and provides a working model for the role of YggS in the maturation of TyrB.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"13 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147752935","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comprehensive and Comparative Transcriptional Profiling of the Cell Wall Stress Response in Bacillus subtilis","authors":"Qian Zhang, Charlène Cornilleau, Lena Friebel, Sarah Spitzner, Raphael R. Müller, Doreen Meier, Pierre Flores, Cyprien Guérin, Pierre Nicolas, Diana Wolf, Vincent Fromion, Rut Carballido‐López, Thorsten Mascher","doi":"10.1111/mmi.70069","DOIUrl":"https://doi.org/10.1111/mmi.70069","url":null,"abstract":"The bacterial cell wall is an essential protective barrier, the frontline of cellular interactions with the environment and also a target for numerous antimicrobial agents. Accordingly, its integrity and homeostasis are closely monitored, and rapid adaptive responses by transcriptional reprogramming induce appropriate counter‐measures against perturbations. Here, we report a comprehensive and comparative transcriptional profiling of the cell envelope stress response (CESR) in the Gram‐positive model bacterium <jats:italic> <jats:styled-content style=\"fixed-case\">Bacillus subtilis</jats:styled-content> , </jats:italic> by integrating RNAseq and high‐resolution tiling array data. We exposed growing cells to a range of antimicrobial compounds that interfere with cytoplasmic, membrane‐coupled or extracellular steps of peptidoglycan (PG) biosynthesis. Transcriptomic studies revealed the complexity of the resulting cell wall stress responses of <jats:styled-content style=\"fixed-case\"> <jats:italic>B. subtilis</jats:italic> </jats:styled-content> and unraveled the contribution of extracytoplasmic function (ECF) sigma factors and two‐component signal transduction systems (TCSs). While membrane‐anchored steps are tightly controlled, early cytoplasmic and late extracellular steps of PG biosynthesis are hardly monitored at all. The ECF <jats:italic>σ</jats:italic> factors <jats:italic>σ</jats:italic> <jats:sup>W</jats:sup> and <jats:italic>σ</jats:italic> <jats:sup>M</jats:sup> both respond to several cell wall synthesis inhibitors and protect the cytoplasmic membrane and cell wall, respectively, while <jats:italic>σ</jats:italic> <jats:sup>V</jats:sup> is almost exclusively induced by lysozyme, against which it provides specific resistance. Remarkably, <jats:italic>σ</jats:italic> <jats:sup>X</jats:sup> was slightly repressed by most antibiotics, pointing towards a role in envelope homeostasis rather than cell wall stress. It shares this role with the essential TCS WalRK, which balances cell wall growth with controlled autolysis. In contrast, all remaining TCSs are envelope stress‐inducible systems. LiaRS is induced by a wide range of PG synthesis inhibitors, while the three paralogous systems BceAB, PsdRS, and ApeRS are more compound‐specific detoxification modules. Induction of the CssRS TCS by all antibiotics interfering with membrane‐anchored steps of PG biosynthesis points toward a physiological link between CESR and secretion stress. Based on the expression signatures, a series of CESR‐specific <jats:styled-content style=\"fixed-case\"> <jats:italic>B. subtilis</jats:italic> </jats:styled-content> whole‐cell biosensors were developed and carefully evaluated. Overall, this comprehensive transcriptomic study establishes a reference framework for future studies of Gram‐positive stress responses triggered by cell wall‐targeting antibiotics.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"319 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147695384","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Redundant and Flexible Electron Transfer Pathways Underlie MsrPQ ‐Mediated Repair of Oxidized Periplasmic Proteins","authors":"Laurent Loiseau, Benjamin Ezraty","doi":"10.1111/mmi.70070","DOIUrl":"https://doi.org/10.1111/mmi.70070","url":null,"abstract":"The MsrPQ system is essential for the repair of oxidized methionine residues in periplasmic proteins, ensuring bacterial resistance to oxidative stress and envelope integrity. While ubiquinones were initially proposed as the primary electron source for MsrPQ, in vitro studies suggested that the flavin reductase Fre and the FMN cofactor of MsrQ are essential for electron transfer from cytoplasmic NADH to MsrP. However, their physiological relevance in vivo remained unclear. Here, we investigated the role of Fre and FMN in the MsrPQ system using <jats:styled-content style=\"fixed-case\"> <jats:italic>Escherichia coli</jats:italic> </jats:styled-content> as a model organism. We demonstrate that deletion of the <jats:italic>fre</jats:italic> gene does not impair MsrPQ activity, as Δ <jats:italic>fre</jats:italic> mutants exhibit wild‐type growth on methionine sulfoxide and maintain normal colony morphology under anaerobic chlorate stress. Additionally, the redox state of periplasmic proteins remains unaffected in Δ <jats:italic>fre</jats:italic> strains, unlike in Δ <jats:italic>msrPQ</jats:italic> mutants where these proteins accumulate in an oxidized form. Furthermore, we show that the MsrQ <jats:sup>H151A</jats:sup> and MsrQ <jats:sup>R77A/R78A</jats:sup> variants, which lack the FMN cofactor and exhibit altered quinone‐binding capacity, respectively, retain full functionality in vivo, albeit with a delayed growth phenotype on methionine sulfoxide. However, we show that Fre becomes necessary for efficient methionine sulfoxide utilization by the MsrPQ system when MsrQ is plasmid‐expressed, and that this dependence is further increased when MsrQ is impaired in ubiquinone binding. These observations indicate that the contribution of Fre is conditionally determined by MsrQ abundance. Collectively, our findings reveal that the MsrPQ system operates through a redundant network of electron transfer pathways, with ubiquinone as a central player. This redundancy likely represents an evolutionary adaptation to ensure robust proteostasis even when specific components of the electron transfer chain are compromised.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"47 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-04-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147666548","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Typhoid Toxin of Salmonella enterica Induces ISG15 Responses Mediating Host Cell Survival and Counteracting Intracellular Infection","authors":"Daniel S. Stark, Michelle King, Angela E. M. Ibler, Salma Srour, Francesca Brown, James Sheffield, Nadia Baseer, Ellen G. Vernon, Yifeng Zhang, Christopher Staples, Lilliana Radoshevich, Daniel Humphreys","doi":"10.1111/mmi.70067","DOIUrl":"https://doi.org/10.1111/mmi.70067","url":null,"abstract":"The typhoid toxin is a secreted virulence factor of typhoidal serovars of the bacterial pathogen <jats:styled-content style=\"fixed-case\"> <jats:italic>Salmonella enterica</jats:italic> </jats:styled-content> implicated in typhoid fever and chronic infections. The toxin causes a DNA damage response in human cells, characterised by cell‐cycle arrest and cellular distension, resulting in cellular senescence and increased bacterial burden. To better understand host responses to typhoid toxin, we performed a transcriptomic analysis of intoxicated host cells and found that the toxin induced expression of genes relating to the type‐I interferon response, including the ubiquitin‐like protein ISG15. ISG15 was upregulated in a STING‐dependent manner, reduced bacterial burden, and was found to be critical to host cell survival in response to the typhoid toxin and interferon. This highlights ISG15 as an important component of the host cell defence to the typhoid toxin.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"1 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-04-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147666547","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Phosphoproteomic Analysis of GAP50-Deficient Parasites Reveals the Inner Membrane Complex Is Involved in Ion Regulation in Toxoplasma gondii.","authors":"Keqin Huang,Lin Zhao,Qian Jiang,Honglin Jia","doi":"10.1111/mmi.70066","DOIUrl":"https://doi.org/10.1111/mmi.70066","url":null,"abstract":"The Alveolata group of organisms is characterized by a vesicular structure located beneath the plasma membrane. In apicomplexa, this structure is known as the inner membrane complex (IMC). The IMC acts as a scaffold during the budding of the daughter parasite and is utilized as a rigid base for the glideosome. In this study, we discovered that the phosphatase activity of GAP50 is crucial for its function in the biogenesis of the IMC. Through further phosphoproteomic analysis of parasites lacking GAP50, we identified that an NIPA family transporter is localized in the IMC. Knocking out TgNIPA1 significantly impairs the robust growth of the parasites. Additionally, expressing TgNIPA1 in a Salmonella strain lacking magnesium transporters could rescue the growth phenotype of bacteria under low magnesium conditions, indicating that it functions as an active magnesium transporter. Our results strongly suggest that the flattened vesicles of the IMC may play important roles in ion regulation in T. gondii.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"96 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2026-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147641783","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}